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O06745

- YITJ_BACSU

UniProt

O06745 - YITJ_BACSU

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Protein

Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase

Gene
yitJ, BSU11010
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

S-methyl-L-methionine + L-homocysteine = 2 L-methionine.
5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H.

Cofactori

FAD By similarity.
Zinc Reviewed prediction.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi200 – 2001Zinc Reviewed prediction
Metal bindingi265 – 2651Zinc Reviewed prediction
Metal bindingi266 – 2661Zinc Reviewed prediction

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. methylenetetrahydrofolate reductase (NAD(P)H) activity Source: UniProtKB-EC
  3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro

GO - Biological processi

  1. methionine biosynthetic process Source: UniProtKB-KW
  2. tetrahydrofolate interconversion Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, Metal-binding, NAD, NADP, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU11010-MONOMER.
UniPathwayiUPA00193.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase
Including the following 2 domains:
Homocysteine S-methyltransferase (EC:2.1.1.10)
Alternative name(s):
S-methylmethionine:homocysteine methyltransferase
5,10-methylenetetrahydrofolate reductase (EC:1.5.1.20)
Gene namesi
Name:yitJ
Ordered Locus Names:BSU11010
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU11010.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 612612Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductasePRO_0000379125Add
BLAST

Proteomic databases

PaxDbiO06745.

Expressioni

Inductioni

Induced by methionine starvation.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU11010.

Structurei

3D structure databases

ProteinModelPortaliO06745.
SMRiO06745. Positions 2-393.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 280280Hcy-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 280280Homocysteine S-methyltransferaseAdd
BLAST
Regioni295 – 6123185,10-methylenetetrahydrofolate reductaseAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the methylenetetrahydrofolate reductase family.
Contains 1 Hcy-binding domain.

Phylogenomic databases

eggNOGiCOG0685.
HOGENOMiHOG000028409.
KOiK00547.
OMAiQSHLMGL.
OrthoDBiEOG6SNDP1.
PhylomeDBiO06745.

Family and domain databases

Gene3Di3.20.20.220. 1 hit.
3.20.20.330. 1 hit.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR003171. Mehydrof_redctse.
IPR003726. S_MeTrfase.
[Graphical view]
PfamiPF02219. MTHFR. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 1 hit.
SSF82282. SSF82282. 1 hit.
PROSITEiPS50970. HCY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O06745-1 [UniParc]FASTAAdd to Basket

« Hide

MGLLEDLQRQ VLIGDGAMGT LLYSYGIDRC FEELNISKPE EIQRIHKAYV    50
EAGANIIQTN TYGANYIKLS RHGLEDDIKK MNQEAVKIAR ASAGDAYVLG 100
TMGGIRTFNK NAYSLDEIKR SFREQLYLLL HEEPDGLLLE TYYDLEEARE 150
VLKIARKETD LPIMLNVSMH EQGVLQDGTP LSDALRSIAD LGADIVGINC 200
RLGPYHMIEA LSEVPIFDDV FLSVYPNSSL PSLEEGRLVY ETDDTYFQNS 250
ASEFRKQGAR IIGGCCGTTP NHIRAMAEAV GGLAPITEKE VKTRAKEFIS 300
VHHERTEPGL DEIAAKKRSI IVELDPPKKL SFDKFLSAAA ELKEAGIDAL 350
TLADNSLATP RISNVACGAL VKQQLDMRSL VHITCRDRNI IGLQSHLMGL 400
DTLGLNDVLA ITGDPSKIGD FPGATSVYDL TSFDLIRLIK QFNEGLSLSG 450
KPLGKKTNFS VAAAFNPNVR HLDKAVKRLE KKIDCGADYF VSQPVYSEQQ 500
LVDIHNETKH LKTPIYIGIM PLTSSRNAEF IHNEIPGIKL SDTIREKMAH 550
AGEDKEKQKA EGLAIARSLL DTACELFNGI YLITPFLRSD LTAELTSYIQ 600
QKDEQRQNIF LH 612
Length:612
Mass (Da):67,928
Last modified:July 1, 1997 - v1
Checksum:iA7B6FFC2E648F800
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09476 Genomic DNA. Translation: CAA70665.1.
AL009126 Genomic DNA. Translation: CAB12941.1.
PIRiC69840.
RefSeqiNP_388982.1. NC_000964.3.
WP_003245847.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB12941; CAB12941; BSU11010.
GeneIDi939796.
KEGGibsu:BSU11010.
PATRICi18973908. VBIBacSub10457_1148.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09476 Genomic DNA. Translation: CAA70665.1 .
AL009126 Genomic DNA. Translation: CAB12941.1 .
PIRi C69840.
RefSeqi NP_388982.1. NC_000964.3.
WP_003245847.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali O06745.
SMRi O06745. Positions 2-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU11010.

Proteomic databases

PaxDbi O06745.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12941 ; CAB12941 ; BSU11010 .
GeneIDi 939796.
KEGGi bsu:BSU11010.
PATRICi 18973908. VBIBacSub10457_1148.

Organism-specific databases

GenoListi BSU11010.

Phylogenomic databases

eggNOGi COG0685.
HOGENOMi HOG000028409.
KOi K00547.
OMAi QSHLMGL.
OrthoDBi EOG6SNDP1.
PhylomeDBi O06745.

Enzyme and pathway databases

UniPathwayi UPA00193 .
BioCyci BSUB:BSU11010-MONOMER.

Family and domain databases

Gene3Di 3.20.20.220. 1 hit.
3.20.20.330. 1 hit.
InterProi IPR029041. FAD-linked_oxidoreductase-like.
IPR003171. Mehydrof_redctse.
IPR003726. S_MeTrfase.
[Graphical view ]
Pfami PF02219. MTHFR. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view ]
SUPFAMi SSF51730. SSF51730. 1 hit.
SSF82282. SSF82282. 1 hit.
PROSITEi PS50970. HCY. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees position encoding 11 membrane proteins."
    Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.
    Microbiology 143:3309-3312(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in Gram-positive bacteria."
    Grundy F.J., Henkin T.M.
    Mol. Microbiol. 30:737-749(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: 168 / BR151.

Entry informationi

Entry nameiYITJ_BACSU
AccessioniPrimary (citable) accession number: O06745
Secondary accession number(s): Q796P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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